Biochem Exam 2

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Alanine

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204 Terms

1

Alanine

Ala, A, Non-polar

<p>Ala, A, Non-polar</p>
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2

Valine

Val, V, Non-polar

<p>Val, V, Non-polar</p>
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3

Phenylalanine

Phe, F, Non-polar

<p>Phe, F, Non-polar</p>
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4

Tryptophan

Trp, W, Non-polar

<p>Trp, W, Non-polar</p>
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5

Leucine

Leu, L, Non-polar

<p>Leu, L, Non-polar</p>
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6

Isoleucine

Ile, I, Non-polar

<p>Ile, I, Non-polar</p>
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7

Methionine

Met, M, Non-polar

<p>Met, M, Non-polar</p>
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8

Proline

Pro, P, Non-polar

<p>Pro, P, Non-polar</p>
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9

Serine

Ser, S, Polar

<p>Ser, S, Polar</p>
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10

Threonine

Thr, T, Polar

<p>Thr, T, Polar</p>
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11

Tyrosine

Tyr, Y, Polar

<p>Tyr, Y, Polar</p>
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12

Asparagine

Asn, N, Polar

<p>Asn, N, Polar</p>
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13

Glutamine

Gln, Q, Polar

<p>Gln, Q, Polar</p>
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14

Cysteine

Cys, C, Polar (creates disulfide bonds with other cysteines

<p>Cys, C, Polar (creates disulfide bonds with other cysteines</p>
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15

Histidine

His, H, Polar (can be charged)

<p>His, H, Polar (can be charged)</p>
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16

Lysine

Lys, K, Basic (pos charge)

<p>Lys, K, Basic (pos charge)</p>
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17

Arginine

Arg, R, Basic (pos charge)

<p>Arg, R, Basic (pos charge)</p>
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18

Aspartate (aspartic acid)

Asp, D, Acidic (neg charge)

<p>Asp, D, Acidic (neg charge)</p>
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19

Glutamate (glutamic acid)

Glu, E, Acidic (neg charge)

<p>Glu, E, Acidic (neg charge)</p>
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20

Glycine

Gly, G, Not charged

<p>Gly, G, Not charged</p>
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21

Rank the following according to their strength as acids--rank from strongest (1) to weakest (5).

A - 4 B - 3 C - 5 D - 2 E - 1

<p>A - 4 B - 3 C - 5 D - 2 E - 1</p>
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22

Which of the following would NOT form a suitable buffer?

Hydrochloric acid/chloride

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23

Under what conditions would a carboxyl group (COOH, pK 3.5) be mostly protonated?

pH < pK

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24

Under what conditions would a carboxyl group (COOH, pK 3.5) be mostly deprotonated?

pH > pK

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25

In aqueous solution, globules of up to several thousand amphiphilic molecules arranged with the hydrophilic groups on the surface and the hydrophobic groups buried in the center are called _____.

micelles

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26

What term is used to describe the exclusion of nonpolar substances from an aqueous solution?

hydrophobic effect

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27

Which of the following is an example of the hydrophobic effect?

all are examples of the hydrophobic effect

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28

A molecule that has both a polar and nonpolar region is called _____________.

amphiphilic

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29

If the pK value for acetic acid (CH3COOH) is 4.76 at what pH would one observe equal amounts of CH3COO- and CH3COOH?

4.76

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30

During metabolic acidosis, ______ ventilation excretes acid in the form of _____ .

increased; CO2

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31

The LOWER the pK value of an acid the STRONGER the acid.

True

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32

Which of the following bond forces are important in tertiary structure:

Hydrophobic effect Hydrogen bonds Disulfide bonds

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33

Which of the following amino acid substitutions would be most likely to effect protein function?

B

<p>B</p>
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34

Select all the commonalities between alpha helices and b-pleated sheets. (i.e. select what is similar in both types of secondary structure)

prolines and glycines aren't suitable for the secondary structure hydrogen bonds between main chain CO and NH groups peptide bond is planar

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35

The formation of a dipeptide from two amino acids involves

A) side-chain complementarity.

B) loss of water.

C) oxidation of the alpha-carbon.

D) reduction of the alpha-carbon.

E) base catalysis.

B

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36

The protein shown above is the human coronavirus protease. The structure contains 2 subunits, that have identical sequences. This protein can be classified as:

quaternary:homodimer

<p>quaternary:homodimer</p>
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37

At what pH would an amino acid bear both a COOH and an NH2 group?

Never

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38

All secondary structures in proteins involve helical forms.

False

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39

Cys-Ala-Gly-Arg-Gln-Met

In the above peptide, the amino-terminal amino acid is ____ and the carboxyl-terminal amino acid is ____

Cys; Met

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40

For the amino acid structures shown above, the protonation state of structure A is shown at ______ pH, and the protonation state of structure B is shown at _______ pH.

low; high

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41

Choose the amino acid that would be more likely to appear on the solvent-exposed (water facing) surface of a protein.

Leu or Lys Ser or Ala Phe or Tyr Trp or Gln Asn or Ile

Lys

Ser

Tyr

Gln

Asn

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42

Primary

The order in which the amino acids in a protein are linked by peptide bonds

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43

Secondary

The arrangement of the backbone atoms in a polypeptide chain

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44

Tertiary

The arrangement of all the atoms in a protein (interactions between the R groups, hydrophobic ones inside of the protein)

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45

Quaternary

the interaction of several polypeptide chains in a multisubunit protein

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46

Examine the four amino acids given below:

Indicate which of these amino acids are associated with the following properties:

branched aliphatic sidechain - C basic sidechain - D aromatic R group - B cyclic (nonaromatic) R group - A

<p>branched aliphatic sidechain  - C basic sidechain  -  D aromatic R group -  B cyclic (nonaromatic) R group  -  A</p>
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47

Which of the following amino acids carry a net positive charge at pH 7.0?

Arg, Lys

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48

What is the net charge on the following peptide at pH 9.5?

Lys-Ala-Glu-Gln-Cys-Ile

-2

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49

What is the net charge of the pentapeptide Ala-Cys-Ser-Glu-Asn at pH 7?

-1

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50

Any peptide which contains 2 sulfur-containing amino acids can form an internal disulfide bond.

False

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51

The interactions that stabilize multisubunit complexes are different than those that stabilize tertiary structure.

False

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52

Myoglobin is _____; hemoglobin is _____.

monomeric; tetrameric

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53

The individual hemoglobin subunits and myoglobin share similar primary structure but have rather different secondary structure.

False

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54

Which of the following fibers is correctly paired with the protein that forms the fiber?

extracellular support fibers: collagen microtubules: tubulin microfilaments: actin intermediate filaments: keratin (all are true)

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55

Which amino acid is critical for crosslinking of keratin fibers?

Cys (disulfide bonds)

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56

The idea that binding of one molecule of oxygen to hemoglobin enhances further binding of oxygen to hemoglobin is called _____.

cooperativity

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57

What is the most prevalent secondary structure observed in the proteins of intermediate filaments?

alpha helices

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58

Which of the following statements about actin are true?

Monomeric G-actin polymerizes to form F-actin. Actin filaments are polar (the ends can be distinguished).

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59

Several oxygen dissociation curves are shown in the figure below. Assuming that curve 3 corresponds to isolated hemoglobin placed in a solution containing physiologic concentrations of CO2 and BPG at a pH of 7.0, indicate which of the curves reflects the following changes in conditions:

Increased BPG concentration 4

Increased pH 2

Dissociation of hemoglobin into subunits. 1

<p>Increased BPG concentration 4</p><p>Increased pH 2</p><p>Dissociation of hemoglobin into subunits. 1</p>
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60

Match the feature of hemoglobin with the proper structural level.

Amino acid sequence in each of the alpha and beta polypeptide chains. Primary Structure

8 alpha helices in each of the subunits. Secondary Structure

Spatial relationship between every atom in the individual subunits. Tertiary Structure

Spatial relationship between the four polypeptide chains. Quaternary Structure

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61

The presence of 2,3-BPG causes hemoglobin's affinity for oxygen to______.

decrease

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62

Which amino acid is involved in heme coordination in both hemoglobin and myoglobin and is highly conserved?

Histidine

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63

Calculate the fractional saturation for myoglobin when pO2 is a. 20 torr and b. 80 torr. Assume K=2.8.

a. 0.88 b. 0.97

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64

Both myoglobin and hemoglobin exhibit cooperative binding to oxygen.

False

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65

Conservative amino acid mutations (i.e. Val to Leu) are likely to affect stability or function of a protein.

False

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66

Which of the following fatty acids have the lowest melting point?

Linoleate (18:2)

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67

Which of the following types of lipids can be found in cell membranes?

glycerophospholipids cholesterol cerebrosides gangliosides

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68

Select the statements the describe fatty acids:

can either be saturated or unsaturated. mostly found with an even number of carbons

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69

In what way(s) do sphingolipids differ from glycerophospholipids?

Sphingolipids are not built on a glycerol backbone. Sphingolipids contain an acyl group attached via an amide bond on the serine potion of the sphingosine.

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70

Show which are characteristics of peripheral membrane proteins and which are characteristics of integral membrane proteins.

peripheral bind to the surface of membranes

integral have transmembrane domains

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71

Which of the following is most likely to be an unnatural fatty acid?

17:3△t9,12,15 (uneven number of carbons)

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72

Sphingosine is not a component of:

glycerophospholipids

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73

Select the fatty acid in each pair that has the higher melting temperature.

16:1c9 or 16:2c9,12

  • 16:1c9

18:0 or 18:1c9

  • 18:0

18:0 or 20:0

  • 20:0

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74

Membranes are generally symmetrical, i.e., the outer face is composed of the same number and types of phospholipids as the inner face.

False

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75

Phospholipids can freely diffuse from the interior leaflet of the plasma membrane to the exterior leaflet without the assistance of enzymes.

False

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76

Triglycerides are fat storage molecules not typically found in membranes.

True

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77

Match the description given with the correct lipid. (Answers may be used more than once)

Primary storage form of lipids. Triacylglycerols.

Provides stability in the plasma membrane. Cholesterol

Isoprene derivative Cholesterol

Commonly found in nervous tissue Sphingomyelin

Sphingosine backbone with several carbohydrates attached Ganglioside

Glycerol backbone with two fatty acyl groups Glycerophospholipid

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78

A membrane's fluidity is largely determined by the percentage of _____________.

unsaturated fats

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79

The concentration of Ca2+ in the endoplasmic reticulum (outside) is 1 mM, and the concentration of Ca2+ in the cytosol (inside) is 0.1 μM. Calculate ΔG at 37°C when the membrane potential is −50 mV (cytosol negative)

-33,388.1

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80

Which of the following is/are true regarding the glucose transporter?

it transports glucose down it's concentration gradient binding of glucose causes a conformational change so that the transporter is never open on both sides of the membrane

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81

Match the transporter (A- blue, B- green, C- light purple) with it's description.

A - Symporter

B - Uniporter

C - Antiporter

<p>A - Symporter</p><p>B - Uniporter</p><p>C - Antiporter</p>
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82

Indicate whether the following compounds are likely to cross a membrane by simple diffusion or facilitated diffusion transport:

aspartic acid facilitated

carbon dioxide simple

glucose facilitated

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83

Which of the following will cause the opening or closing of a gated ion channel?

voltage change

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84

What substance will be transported through an aquaporin?

water

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85

In the sodium-potassium pump:

sodium is transported out of the cell and potassium into the cell, both against concentration gradients

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86

Active transport is uniquely characterized by:

the tight coupling of an input of energy, with the species going from a lesser concentration to a greater concentration.

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87

Facilitated (Mediated) diffusion across a biological membrane:

is driven by a difference in solute concentration.

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88

Energy requiring transport mechanisms include

Active transport

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89

Inside a nerve cell at rest, [Na +] is ____ and [K+] _____ relative to the concentrations seen outside the cell.

low, high

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90

The Hydrophobic Effect

The exclusion of nonpolar substances from an aqueous solution

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91

Amphiphilic

experience both hydrophilic interactions and the hydrophobic effect. most lipids are amphiphilic.

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92

the pH scale

knowt flashcard image
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93

The ionization of water can be described by a dissociation constant, K:

(products)/(reactants)

<p>(products)/(reactants)</p>
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94

acid

substance that can donate a proton

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95

base

a substance that can accept a proton

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96

pK helps to

determine the strength of an acid (lower pK = stronger acid, higher pK = weaker acid)

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97

Henderson-Hasselbalch Equation

*pK is the specific pH where there are equal concentrations of base and acid *log > 1 --> always positive, pH rises *log < 1 --> always negative, pH lowers

<p>*pK is the specific pH where there are equal concentrations of base and acid *log &gt; 1 --&gt; always positive, pH rises *log &lt; 1 --&gt; always negative, pH lowers</p>
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98

pH < pK

everything will be protonated

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99

buffer

weak acid/conj base system aids in resisting changes in the pH of a system

<p><em>weak acid/conj base system</em> aids in resisting changes in the pH of a system</p>
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100

Amino Acids (L and D groups)

L --> amino group to the left of the alpha carbon D --> amino group to the right of the alpha carbon

L is the most common in nature

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